Paramagnetic Ion Induced Perturbations in the 1H NMR Spectrum of Lysozyme: A Reassignment of the Tryptophan Indole NH Resonances

R. E. Lenkinski, J. L. Dallas, J. D. Glickson

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18 Scopus citations


In H2O the 360-MHz 1H NMR spectrum of the egg white lysozyme, an enzyme which has six tryptophan residues, contains only five resolvable indole N H resonances. These peaks have been assigned to specific tryptophan residues on the basis of the shift perturbations induced by Co2+ and line broadenings induced by Gd3+. Since each of these perturbations obeys a different geometric relationship, the agreement of the two sets of assignments provides a check of the overall method. The results of inhibitor binding studies, chemical modification experiments, and deuterium isotope exchange rates are discussed in terms of the new assignments. Apart from any specific conclusions reached on HEW lysozyme it is clear that for many macromolecules the line broadenings induced by Gd3+ can be analyzed in terms of absolute metal proton distances. In making these assignments we have made use of the crystallographic data for HEW lysozyme. In general, the application of the methodology presented here is restricted to those biomolecules whose structure has been determined by an independent method.

Original languageEnglish (US)
Pages (from-to)3071-3077
Number of pages7
JournalJournal of the American Chemical Society
Issue number11
StatePublished - Jan 1 1979

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry


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